DE102010063743A1 - Liquid surfactant preparation containing lipase and phosphonate - Google Patents

Abstract

A phosphonate-containing liquid surfactant preparation should have a beneficial lipolytic activity. This is achieved by the use of a lipase, which is naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus.

Description

The invention is in the field of liquid enzyme-containing surfactant preparations, as used for example in washing, cleaning or disinfecting. More particularly, the invention relates to liquid enzyme-containing surfactant formulations containing defined lipases in combination with a phosphonate, and further proposes uses and methods in which such formulations are employed. The invention further relates to uses of defined lipases in liquid surfactant formulations containing a phosphonate.

In surfactant preparations, especially in modern liquid detergents, but also in cleaning or disinfecting agents, phosphonates are often included. They are used, for example, as complexing agents, to prevent precipitation or as a bleach stabilizer. As complexing agents they serve, for example, as water softeners. They can encase cations such as Ca ²⁺ in the solution and thus alter the chemical behavior of the cation. In the case of calcium, the property of water hardness disappears. Other cations can be complexed and thus protected against chemical reactions. They can also participate as corrosion inhibitors or serve as a stabilizer for peroxides, especially in bleaching agents.

Furthermore, lipase is increasingly used in surfactant preparations, in particular in detergents or cleaners. A lipase is an enzyme that catalyzes the hydrolysis of ester bonds in lipid substrates, especially in fats and oils. Lipases are therefore a group of esterases. Lipases are generally versatile enzymes that accept a variety of substrates, for example, aliphatic, alicyclic, bicyclic and aromatic esters, thioesters and activated amines. Lipases act against fat residues in the laundry to catalyze their hydrolysis (lipolysis). Lipases with broad substrate spectra are used in particular where inhomogeneous raw materials or substrate mixtures have to be reacted, for example in detergents and cleaners, since soiling may consist of differently structured fats and oils. The lipases used in the washing or cleaning agents known from the prior art are usually of microbial origin and are usually derived from bacteria or fungi, for example the genera Bacillus, Pseudomonas, Acinetobacter, Micrococcus, Humicola, Trichoderma or Trichosporon. Lipases are usually produced by biotechnological methods known per se by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi.

In the European patent application EP 443063 is, for example, intended for detergents and cleaners lipase from Pseudomonas sp. ATCC 21808, but not explicitly for use in a phosphonate-containing liquid formulation. In the Japanese patent application JP 1225490 is a lipase from Rhizopus oryzae disclosed. However, this document also does not disclose a specific liquid surfactant preparation which necessarily contains a phosphonate in combination with a Rhizopus oryzae lipase.

In general, only selected lipases are suitable for use in liquid surfactant preparations. Many lipases do not show sufficient catalytic performance or stability in such formulations. In phosphonate-containing liquid surfactant preparations, this problem is even more serious, for example due to the complex-forming properties of the phosphonates or due to unfavorable interactions between the phosphonate and the lipase.

Consequently, lipase-containing liquid surfactant preparations of the prior art, in particular those containing phosphonates, have the disadvantage that they often do not have satisfactory lipolytic activity and therefore the surfactant preparation does not show optimal cleaning performance on lipase-sensitive soils.

The object of the present invention is to overcome the mentioned disadvantage and to provide a phosphonate-containing liquid surfactant preparation which has a beneficial lipolytic activity.

An object of the invention is a liquid surfactant preparation comprising a phosphonate and a lipase which is naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus.

Surprisingly, it has been found that a liquid surfactant preparation containing the combination of such a lipase with a phosphonate, advantageous cleaning performance at lipase has sensitive stains. Advantageously, such a surfactant preparation exhibits an improved cleaning performance on at least one, preferably on several lipase-sensitive stains, in particular on textiles and / or hard surfaces. In a preferred embodiment, a surfactant preparation according to the invention is also advantageously storage-stable. Further preferred embodiments of surfactant preparations according to the invention show advantageous cleaning performance with regard to at least one lipase-sensitive soiling at temperatures between 10.degree. C. and 80.degree. C., preferably also at low temperatures, for example between 10.degree. C. and 50.degree. C., between 10.degree. C. and 40.degree C or between 20 ° C and 40 ° C. With regard to the prior art mentioned in the introduction, the present invention is therefore a particularly advantageous selection of a lipase for a phosphonate-containing liquid surfactant preparation.

In the context of the invention, cleaning performance is understood to mean the whitening performance of one or more soiling, in particular laundry soiling or scrape dirt, which are sensitive to degradation by the lipase. Examples of such stains are carbon black / mineral oil, carbon black / olive oil, pigment / oil or skin fat (sebum) / carbon black, in each case for example on cotton fabric, in particular as indicated below. In the context of the invention, both the surfactant preparation, which comprises the lipase or the washing or cleaning liquor formed by this surfactant preparation, and the lipase itself have a respective cleaning performance. The cleaning performance of the lipase thus contributes to the cleaning performance of the surfactant preparation or the washing or cleaning liquor formed by the surfactant preparation. The cleaning performance is preferably determined as indicated below.

Washing or cleaning liquor is understood as meaning the use solution containing the surfactant preparation which acts on textiles or fabrics (wash liquor) or hard surfaces (cleaning liquor) and thus comes into contact with the soiling present on textiles or fabrics or hard surfaces. Usually, the washing or cleaning liquor arises when the washing or cleaning process begins and the surfactant preparation, in particular the detergent or cleaning agent, for example, in a washing machine, dishwasher or other suitable container is diluted with water.

A lipase contained in a surfactant preparation according to the invention has a lipolytic activity, that is, it is capable of hydrolysis (lipolysis) of lipids such as glycerides or cholesterol esters. Furthermore, the lipase contained in a surfactant preparation according to the invention is naturally present in a microorganism of the species Rhizopus oryzae or Mucor javanicus. Naturally present in this context means that the lipase is a separate enzyme of the microorganism. The lipase can thus be expressed in the microorganism from a nucleic acid sequence which is part of the chromosomal DNA of the microorganism in its wild-type form. It or the coding for them nucleic acid sequence is therefore present in the wild-type form of the microorganism and / or can be isolated from the wild-type form of the microorganism from this. In contrast to this, a lipase not present in the microorganism or the nucleic acid sequence coding for it would have been deliberately introduced into the microorganism with the aid of genetic engineering, so that the microorganism would have been enriched by the lipase or the nucleic acid sequence coding for it. However, a lipase naturally present in a microorganism of the genus Rhizopus oryzae or Mucor javanicus may well have been produced recombinantly from another organism.

The fungus Rhizopus oryzae belongs to the class of Zygomycetes (subclass Incertae sedis), herein to the order Mucorales and here again to the family Mucoraceae and the genus Rhizopus. The fungus Mucor javanicus also belongs to the class of Zygomycetes (subclass Incertae sedis), herein to the order Mucorales and here again to the family Mucoraceae, then herein to the genus Mucor. The names Rhizopus oryzae and Mucor javanicus are the biological species names within the respective genus.

Phosphonates are salts and organic compounds, especially esters, of phosphonic acid. As salts there exist primary (M'H ₂ PO ₃ or HP (O) (OH) (OM ')) and secondary (M' ₂ HPO ₃ or HP (O) (OM ') ₂ ) phosphonates, where M' stands for a monovalent metal. These inorganic phosphonates are also referred to as primary and secondary phosphites, respectively. Inorganic phosphonates are formed, for example, by reaction of phosphonic acid HP (O) (OH) ₂ , in particular the stable tautomeric form of phosphorous acid with a (primary) or two (secondary) equivalents of base, for example alkali metal hydroxide.

In the context of the present invention, preference is given to organic P-substituted phosphonates which have a phosphorus-carbon bond (phosphorus-organic compounds). Their general structure is R1P (O) (OR2) ₂ , with R1 and / or R2 = alkyl, aryl or H, where the alkyl or aryl radicals are further substitutions or may carry additional chemical groups. Organic P-substituted phosphonates are formed, for example, by the Michaelis-Arbusov reaction. Many of these phosphonates are soluble in water. Some technically important phosphonates also carry amino group (s). Some of these aminophosphonates have structural similarities to complexing agents such as EDTA, NTA or DTPA and have a similar function.

Particularly preferred phosphonates in the context of the present invention are 1-hydroxyethane-1,1-diphosphonic acid (HEDP), aminotrimethylenephosphonic acid (ATMP), nitrilotrimethylenephosphonic acid (NTMP), diethylenetriaminepentamethylenephosphonic acid (DTPMP, DETPMP or DTPNT), ethylenediamine tetramethylenephosphonic acid (EDTMP) and 2-phosphonobutane. 1,2,4-tricarboxylic acid (PBS-AM, also referred to as 3-carboxy-3-phosphonoadipic acid), which are usually used in the form of their ammonium or alkali metal salts. Furthermore, combinations of the phosphonates can be used.

Particular preference is given to diethylenetriaminepentamethylenephosphonic acid sodium (DTPMP), in particular for surfactant preparations according to the invention which are detergents, and / or 1-hydroxyethane-1,1-diphosphonic acid (HEDP), in particular for surfactant preparations according to the invention which contain washing or dishwashing detergents, in particular automatic dishwasher detergents, represent. Such phosphonates are, for example, under the trade name Dequest ^® 2066 and Dequest ^® 2010 (each company Thermphos) available.

In a further embodiment of the invention, the surfactant preparation is characterized in that the lipase has an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 amino acid sequence is at least 80% identical. More preferably, the amino acid sequence is at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95% %, 96%, 97%, 98%, 99% and most preferably 100% identical to that shown in SEQ ID NO. 1 indicated amino acid sequence. SEQ ID NO. 1 is the sequence of a mature (mature) lipase from Rhizopus oryzae.

According to most preferred lipases are those of the company Amano Pharmaceuticals under the names Lipase M-AP10 ^®, Lipase LE ^® and Lipase F ^® lipase enzymes (including lipase JV ^®) available. For example, the ^{Lipase F®} is naturally present in Rhizopus oryzae. The lipase M-AP10 ^®, for example, naturally present in Mucor javanicus.

According to the invention, it has been found that the addition of such a lipase to a liquid surfactant preparation which comprises a phosphonate, in particular one as described above, provides a particularly advantageous lipolytic activity in this preparation. Furthermore, such surfactant preparations are sufficiently stable on storage, in particular with regard to their remaining lipolytic activity after storage, in particular after a storage period of 1 to 5 weeks, 1 to 4 weeks, 1.5 to 3 weeks and particularly preferably after 2 weeks.

Particularly preferred combinations of lipase and phosphonate in surfactant preparations according to the invention are:
Lipase having an amino acid sequence corresponding to that shown in SEQ ID NO. At least 80% and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, 99%, and most preferably 100% identical in combination with 1-hydroxyethane-1,1-diphosphonic acid (HEDP);
Lipase having an amino acid sequence corresponding to that shown in SEQ ID NO. At least 80% and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, 99%, and most preferably 100% identical in combination with aminotrimethylene phosphonic acid (ATMP);
Lipase having an amino acid sequence corresponding to that shown in SEQ ID NO. At least 80% and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, 99% and most preferably 100% identical in combination with nitrilotrimethylene phosphonic acid (NTMP);
Lipase having an amino acid sequence corresponding to that shown in SEQ ID NO. At least 80% and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, 99%, and most preferably 100% identical in combination with diethylenetriaminepentamethylenephosphonic acid (DTPMP);
Lipase having an amino acid sequence corresponding to that shown in SEQ ID NO. At least 80% and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, 99% and most preferably 100% identical in combination with ethylenediamine tetramethylene phosphonic acid (EDTMP);
Lipase having an amino acid sequence corresponding to that shown in SEQ ID NO. At least 80% and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, 99%, and most preferably 100% identical in combination with 2-phosphonobutane-1,2,4-tricarboxylic acid (PBS-AM);
Lipase M-AP10 ^® in combination with 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or aminotrimethylenephosphonic acid (ATMP) or nitrilotrimethylenephosphonic acid (NTMP) or diethylenetriaminepentamethylenephosphonic acid (DTPMP) or ethylene diamine tetramethylene phosphonate (EDTMP) or 2-phosphonobutane-1,2,4 tricarboxylic acid (PBS-AM);
Lipase LE ^® in combination with 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or aminotrimethylenephosphonic acid (ATMP) or nitrilotrimethylenephosphonic acid (NTMP) or diethylenetriaminepentamethylenephosphonic acid (DTPMP) or ethylene diamine tetramethylene phosphonate (EDTMP) or 2-phosphonobutane-1,2,4-tricarboxylic (PBS-AM);
Lipase F ^® in combination with 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or aminotrimethylenephosphonic acid (ATMP) or nitrilotrimethylenephosphonic acid (NTMP) or diethylenetriaminepentamethylenephosphonic acid (DTPMP) or ethylene diamine tetramethylene phosphonate (EDTMP) or 2-phosphonobutane-1,2,4-tricarboxylic (PBS-AM).

The identity of nucleic acid or amino acid sequences is determined by a sequence comparison. Such a comparison is made by assigning similar sequences in the nucleotide sequences or amino acid sequences to each other. This sequence comparison is preferably carried out based on the BLAST algorithm established and commonly used in the prior art (cf., for example, US Pat Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." J. Mol. Biol. 215: 403-410 , and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs "; Nucleic Acids Res., 25, pp. 3389-3402 ) and in principle takes place in that similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences are assigned to one another. A tabular assignment of the respective positions is referred to as alignment. Another algorithm available in the prior art is the FASTA algorithm. Sequence comparisons (alignments), in particular multiple sequence comparisons, are usually created using computer programs. Frequently used, for example, the Clustal series (see, for example Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 ), T-Coffee (cf., for example Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217 ) or programs based on these programs or algorithms. For example, Clustal (cf., for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 ) or T-Coffee (cf., for example Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217 ) as well as BLAST or FASTA for the database search, or programs based on these programs or algorithms. In the present invention, sequence comparisons and alignments (1600 Faraday Avenue, Carlsbad, California, United States Invitrogen Corporation) are preferred to the computer program Vector NTI ^® Suite 10.3 created with the preset default parameters.

Such a comparison allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is, the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions. The broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar chemical activity, as these usually perform similar chemical activities within the protein. Therefore, the similarity of the sequences compared may also be stated as percent homology or percent similarity. Identity and / or homology information can be made about whole polypeptides or genes or only over individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. Such areas often have identical functions. They can be small and comprise only a few nucleotides or amino acids. Often, such small regions exert essential functions for the overall activity of the protein. It may therefore be useful to relate sequence matches only to individual, possibly small areas. Unless stated otherwise, identity or homology information in the present application, however, refers to the total length of the respectively indicated nucleic acid or amino acid sequence.

• – Ruß/Mineralöl auf Baumwolle: Produkt Nr. C-01 erhältlich von CFT (Center For Testmaterials) B. V. Vlaardingen, Niederlande
• – Ruß/Olivenöl auf Baumwolle: Produkt Nr. C-02 erhältlich von CFT (Center For Testmaterials) B. V. Vlaardingen, Niederlande
• – Pigment/Öl auf Baumwolle: Produkt Nr. C-09 erhältlich von CFT (Center For Testmaterials) B. V. Vlaardingen, Niederlande
• – Hautfett (Sebum)/Kohlenschwarz, auf Baumwolle: Produkt Nr. C-S-32 erhältlich von CFT (Center For Testmaterials) B. V. Vlaardingen, Niederlande,

bestimmt wird durch Messung des Weißheitsgrades der gewaschenen Textilien, der Waschvorgang für mindestens 30 Minuten, optional 60 Minuten, bei einer Temperatur von 40°C erfolgt und das Wasser eine Wasserhärte zwischen 15,5 und 16,5° (deutsche Härte) aufweist.In a further embodiment of the invention, a surfactant preparation according to the invention is further characterized in that its cleaning performance is at least that of a surfactant preparation corresponding to a lipase which has an amino acid sequence according to SEQ ID NO. 1, wherein the cleaning performance is determined in a washing system containing a detergent in a dosage between 2.0 and 9.0 grams per liter of wash liquor and the lipase, wherein the lipases to be compared are used in the same activity and the cleaning performance against one or more Soil / mineral oil stains on cotton, soot / olive oil on cotton, pigment / oil on cotton or skin fat (sebum) / carbon black, on cotton, in particular against one or more stains

• - Carbon black / mineral oil on cotton: Product No. C-01 available from CFT (Center For Test Materials) BV Vlaardingen, The Netherlands
• - Carbon black / olive oil on cotton: Product No. C-02 available from CFT (Center For Test Materials) BV Vlaardingen, The Netherlands
• - Pigment / Oil on cotton: Product No. C-09 available from CFT (Center For Test Materials) BV Vlaardingen, The Netherlands
• - Skin fat (sebum) / carbon black, on cotton: Product No. CS-32 available from CFT (Center For Test Materials) BV Vlaardingen, The Netherlands,

is determined by measuring the whiteness of the washed textiles, the washing process for at least 30 minutes, optionally 60 minutes, at a temperature of 40 ° C and the water has a water hardness between 15.5 and 16.5 ° (German hardness).

The detergent for the washing system is a liquid detergent composed as follows (all figures in weight percent): 0.3-0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerin , 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% Coconut fatty acids, 0.5% HEDP (1-hydroxyethane-1,1-diphosphonic acid), 0-0.4% PVP (polyvinylpyrrolidone), 0-0.05% optical brightener, 0-0.001% dye, balance demineralized water , The lipase is used in this regard in a concentration of 0.0001-0.06 wt .-%, preferably from 0.001 to 0.006 wt .-%, in the detergent, based on active protein. The dosage of the liquid detergent is between 2.0 and 9.0, preferably between 2.5 and 8.0, between 3.0 and 7.0 and more preferably 3.5 grams per liter of wash liquor. Washing takes place in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9. The lipase activity in the wash liquor is not equal to zero at the start of washing.

The degree of whiteness, d. H. the brightening of the stains, as a measure of the cleaning performance is determined by optical measurement methods, preferably photometrically. A suitable device for this purpose is for example the spectrometer Minolta CM508d. Usually, the devices used for the measurement are previously calibrated with a white standard, preferably a supplied white standard.

The activity-like use of the respective lipase ensures that even if the ratio of active substance to total protein (the values of the specific activity) diverge, the respective enzymatic properties, for example the cleaning performance of certain soils, are compared. In general, a low specific activity can be compensated by adding a larger amount of protein.

The lipase activity is determined in the usual way, preferably as described in US Pat Bruno Stellmach, "Methods of Determination Enzymes for Pharmacy, Food Chemistry, Technology, Biochemistry, Biology, Medicine" (Steinkopff Verlag Darmstadt, 1988, p. 172 ff) , In this case, lipase-containing samples are added to an olive oil emulsion in emulsifier-containing water and incubated at 30 ° C and pH 9.0. This fatty acids are released. These are done with an autotitrator over 20 min. titrated continuously with 0.01 N sodium hydroxide solution so that the pH remains constant ("pH-stat titration"). Based on the sodium hydroxide consumption, the determination of the lipase activity takes place by reference to a reference lipase sample.

Numerous lipases are formed as so-called pre-proteins, ie together with a propeptide and / or a signal peptide. Often the prodrug and / or signal peptide are N-terminal sequences. In the course of the folding and / or secretion process of the protein signal and / or propeptide are cleaved, so that after the cleavage of the pro- and / or signal peptide, the then mature lipase their catalytic activity without the originally present N-terminal amino acids exercises. For technical applications in general and in particular in the context of the invention, the mature (mature) lipases, ie the enzymes processed after their preparation, are preferred over the preproteins. The lipases can also be modified by the cells producing them after the polypeptide chain has been produced, for example by attachment of sugar molecules, formylations, aminations, etc. Such Modifications are posttranslational modifications and may, but do not necessarily, have an impact on the function of the lipase.

Furthermore, the lipase contained in a surfactant preparation according to the invention may be adsorbed to carriers and / or embedded in encapsulating substances in order to protect them against premature inactivation. In the washing or cleaning liquor, ie under conditions of use, the lipase is then released and can develop their lipolytic action.

In a preferred embodiment of the invention, the surfactant preparation is characterized in that the phosphonate is contained in an amount of 0.01 to 4 wt .-%. Further preferred amounts of the phosphonate contained in the surfactant preparation are from 0.01 to 3% by weight, from 0.01 to 2.5% by weight, from 0.02 to 2.4% by weight, from 0, 02 to 2 wt .-%, from 0.03 to 1.5 wt .-% or from 0.05 to 1 wt .-%.

The lipase is preferably contained in a surfactant preparation according to the invention in each case in an amount of 1 × 10 ^-8 to 5 wt .-% based on active protein. More preferably, the lipase is in an amount of 1 × 10 ^-7 -3 wt .-%, of 0.00001-1 wt .-%, of 0.0002-0.8% wt .-% and particularly preferably of 0 , 0008-0.4% wt .-% in a surfactant preparations according to the invention, based on active protein. The protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ). The Aktivenzymproteinehalt can by means of "Active Site" titration of the lipase preparation according to Rotticci et al .: "An active site titration method for lipases" (Biochim Biophys Acta 1483 (1), page 132-140) be determined. Here, various concentrations of the enzyme in an appropriate buffer system with an excess of inhibitor (methyl p-nitrophenyl-n-hexylphosphonat) provided and the liberated amount of p-nitrophenolate determined by spectrophotometry at 400 nm.

For the purposes of the present invention, a surfactant preparation is to be understood as meaning any type of composition which comprises at least one surfactant. Preferably, such a composition contains a surfactant as described below.

In this case, all liquid or flowable administration forms can serve as liquid surfactant preparations. "Flowable" in the context of the present application are preparations which are pourable and can have viscosities of up to several tens of thousands of mPas. The viscosity can be measured by conventional standard methods (for example, Brookfield LVT-II viscosimeter at 20 rpm and 20 ° C., spindle 3) and is preferably in the range from 5 to 10,000 mPas. Preferred surfactant formulations have viscosities of 10 to 8000 mPas, with values between 120 to 3000 mPas being particularly preferred. A liquid surfactant preparation in the context of the present invention can therefore also be gelatinous or paste-like, it can be in the form of a homogeneous solution or suspension, and can be sprayed or packaged in other conventional dosage forms, for example.

A liquid surfactant preparation according to the invention can be used as such or after dilution with water, in particular for the cleaning of textiles and / or hard surfaces. Such a dilution can be readily prepared by diluting a measured amount of the surfactant preparation in a further amount of water in certain weight ratios of surfactant preparation: water and optionally shaking this dilution to ensure even distribution of the surfactant formulation in the water. Possible weight or volume ratios of the dilutions are from 1: 0 surfactant preparation: water to 1: 10,000 or 1: 20000 surfactant preparation: water, preferably from 1:10 to 1: 2000 surfactant preparation: water.

A surfactant preparation in the sense of the present invention can therefore also be the washing or cleaning liquor itself.

In a preferred embodiment, the surfactant preparation is a washing, cleaning or disinfecting agent. The detergents include all conceivable types of detergents, in particular detergents for textiles, carpets or natural fibers. They can be provided for manual and / or machine application. The detergents also include washing aids, which are added to the actual detergent in the manual or machine textile washing, in order to achieve a further effect. Detergents include all agents for cleaning and / or disinfecting hard surfaces also found in all of the above dosage forms, manual and automatic dishwashing detergents, carpet cleaners, abrasives, glass cleaners, toilet scavengers, etc. Textilvor- and Aftertreatment agents are on the one hand such agents with which the laundry item is brought into contact before the actual laundry, for example, to dissolve stubborn soiling, on the other hand, those in a laundry downstream of the laundry further desirable properties such as pleasant Give grip, crease resistance or low static charge. Amongst others, the fabric softeners are calculated. Disinfectants are, for example, hand disinfectants, surface disinfectants and instrument disinfectants, which may also occur in the mentioned dosage forms. A disinfectant preferably causes a germ reduction by a factor of at least 10 ⁴ , that is to say that of originally 10,000 proliferating germs (so-called colony-forming units - CFU) survives no more than a single, with viruses in this regard are not considered as germs, since they have no cytoplasm and have no own metabolism. Preferred disinfectants cause a germ reduction by a factor of at least 10 ⁵ .

As surfactant (s) it is possible to use anionic, nonionic, zwitterionic and / or amphoteric surfactants. From an application point of view, preference is given to mixtures of anionic and nonionic surfactants. The total surfactant content of the liquid surfactant preparation is preferably below 60% by weight, and more preferably below 45% by weight, based on the total liquid surfactant formulation.

Suitable nonionic surfactants include alkoxylated fatty alcohols, alkoxylated fatty acid alkyl esters, fatty acid amides, alkoxylated fatty acid amides, polyhydroxy fatty acid amides, alkylphenol polyglycol ethers, amine oxides, alkyl polyglucosides, and mixtures thereof.

The nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary, alcohols having preferably 8 to 18 carbon atoms and on average 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position or linear and methyl-branched radicals in the mixture can contain, as they are usually present in Oxoalkoholresten. In particular, however, alcohol ethoxylates with linear radicals of alcohols of native origin having 12 to 18 carbon atoms, for example of coconut, palm, tallow or oleyl alcohol, and on average 2 to 8 EO per mole of alcohol are preferred. The preferred ethoxylated alcohols include, for example, C _12-14 alcohols with 3 EO, 4 EO or 7 EO, C _9-11 alcohols with 7 EO, C _13-15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C _12-16 -alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C _12-14 -alcohol with 3 EO and C _12-18 -alcohol with 7 EO. The degrees of ethoxylation given represent statistical means which, for a particular product, may be an integer or a fractional number. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO. Nonionic surfactants containing EO and PO groups together in the molecule can also be used according to the invention. Also suitable are also a mixture of a (more) branched ethoxylated fatty alcohol and an unbranched ethoxylated fatty alcohol, such as a mixture of a C _16-16 fatty alcohol with 7 EO and 2-propylheptanol with 7 EO. Particularly preferably, the surfactant preparation contains a C _12-16 fatty alcohol with 7 EO or a C _13-15 oxo alcohol with 7 EO as nonionic surfactant.

The content of nonionic surfactants is preferably 3 to 40 wt .-%, preferably 5 to 30 wt .-% and in particular 7 to 20 wt .-%, each based on the total surfactant.

In addition to the nonionic surfactants, the surfactant preparation may also contain anionic surfactants. The anionic surfactant used is preferably sulfonates, sulfates, soaps, alkyl phosphates, anionic silicone surfactants and mixtures thereof.

The surfactants of the sulfonate type are preferably C _9-13 -alkylbenzenesulfonates, olefinsulfonates, ie mixtures of alkene and hydroxyalkanesulfonates and disulfonates, as are obtained, for example, from C _12-18 -monoolefins having terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acid hydrolysis of the sulfonation products into consideration. Also suitable are C _12-18 alkanesulfonates and the esters of α-sulfo fatty acids (ester sulfonates), for example the α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

Alk (en) ylsulfates are the alkali metal salts and in particular the sodium salts of the sulfuric monoesters of C ₁₂ -C ₁₈ fatty alcohols, for example coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C ₁₀ -C ₂₀ oxo alcohols and those half-esters of secondary alcohols of these Chain lengths are preferred. Of washing technology interest, the C ₁₂ -C ₁₆ alkyl sulfates and C ₁₂ -C ₁₅ alkyl sulfates and C ₁₄ -C ₁₅ alkyl sulfates are preferred. 2,3-alkyl sulfates are also suitable anionic surfactants.

The sulfuric acid monoesters of straight-chain or branched C _7-21 -alcohols ethoxylated with from 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C _8-11 -alcohols containing on average 3.5 mol of ethylene oxide (EO) or C _12-18 . Fatty alcohols with 1 to 4 EO are suitable.

Also preferred anionic surfactants are soaps. Suitable are saturated and unsaturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, (hydrogenated) erucic acid and behenic acid and, in particular, soap mixtures derived from natural fatty acids, for example coconut, palm kernel, olive oil or tallow fatty acids.

The anionic surfactants including the soaps may be in the form of their sodium, potassium or magnesium or ammonium salts. Preferably, the anionic surfactants are in the form of their sodium salts. Further preferred counterions for the anionic surfactants are also the protonated forms of choline, triethylamine or methylethylamine.

The content of a surfactant preparation of anionic surfactants can be from 1 to 40% by weight, preferably from 5 to 30% by weight and very particularly preferably from 10 to 25% by weight, based in each case on the total surfactant preparation.

• i. anionische und/oder polyanionische Substanz, und/oder
• ii. kationische und/oder polykationische Substanz, und/oder
• iii. Hydroxyl- und/oder Polyhydroxyl-Gruppe(n) aufweisende Substanz.

In a further embodiment of the invention, the surfactant preparation is characterized by further comprising a component selected from

• i. anionic and / or polyanionic substance, and / or
• ii. cationic and / or polycationic substance, and / or
• iii. Hydroxyl and / or polyhydroxyl group (s) having substance.

It has been found that the addition of such substances further improves the cleaning performance of surfactant preparations, in particular of liquid detergents or cleaners containing a lipase, in particular such as described above, in particular at a temperature between 10 ° C and 80 ° C and preferably at comparatively low temperatures, in particular between 10 ° C and 50 ° C, between 10 ° C and 40 ° C, between 10 ° C and 30 ° C and / or between 20 ° C and 40 ° C.

In the case under i. specified substances are anionic or polyanionic substances, d. H. these substances carry at least one and preferably several negative charges. It is preferably a polymer having at least one negatively charged monomer, preferably having a plurality of negatively charged monomers. According to the invention, this polymer is therefore a negatively charged polymer. For example, polymers of organic acids or their salts, in particular polyacrylates and / or poly-sugar acids and / or polyarcylate copolymers and / or poly-sugar copolymers, are preferred. In this regard, further preferred compounds are polyacrylic sulfonates or polycarboxylates and their salts, copolymers or salts of the copolymers.

Examples of particularly preferable substances to be used are Acusol 587D (polyacrylic sulfonate, Rohm & Haas / Dow Chemical Company), Acusol 445N (polycarboxylate sodium salt, Rohm & Haas / Dow Chemical Company), Acusol 590 (polyacrylate copolymer; Rohm & Haas / Dow Chemical ), Acusol 916 (polyarcrylate sodium salt, Rohm & Haas / Dow Chemical Company), Sokalan CP42 (modified polycarboxylate sodium salt, BASF Company), Sokalan PA 30CL (polycarboxylate sodium salt, BASF Company), Dequest P 9000 (polymaleic acid, Thermphos Company), alginic acid Poly-2-acrylamido-2-methyl-1-propanesulfonic acid, poly-4-styrenesulfonic acid-co-maleic acid sodium salt, poly-acrylamido-co-acrylic acid sodium salt, poly-methacrylic acid sodium salt, poly-methyl vinyl ether-old maleic acid or Polyvinylsulfonic acid sodium salt.

In the under ii. Cited substances are cationic or polycationic substances, d. H. these substances carry at least one and preferably several positive charges. It is preferably a polymer having at least one positively charged monomer, preferably having a plurality of positively charged monomers. According to the invention, this polymer is therefore a positively charged polymer. Examples of preferred compounds in this regard are salts of polyamines, polyethylene imines or their copolymers, salts of polyallylamines, salts of Polydiallyldimethylammonium compounds or poly (acrylamide-co-diallyldimethylammonium compounds.

In the under iii. specified substances are substances which have at least one hydroxyl and / or polyhydroxyl group and preferably more hydroxyl and / or polyhydroxyl groups. Preferred in this regard are, for example, polyvinyl alcohols, for example those which are available under the trade name Mowiol (Kremer Pigmente GmbH & Co. KG).

It is expressly noted at this point that a specific substance to one or more of the above groups i. to iii. may be associated. For example, it may be an anionic polymer having one or more hydroxyl and / or polyhydroxyl group (s). Such a substance is then associated with the groups i. and iii. Likewise, a cationic polymer having one or more hydroxyl and / or polyhydroxyl group (s) belonging to the groups ii. and iii.

Also usable in the context of the present invention are derivatives of those mentioned above as belonging to i., Ii. or iii. mentioned substances. For the purposes of the present application, a derivative is understood as meaning a substance which is chemically modified starting from one of the abovementioned substances, for example by the conversion of a side chain or by covalent bonding of another compound to the substance. Such a compound may be, for example, low molecular weight compounds such as lipids or mono-, oligo- or polysaccharides or amines or amine compounds. Further, the substance may be glycosylated, hydrolyzed, oxidized, N-methylated, N-formylated, N-acetylated or methyl, formyl, ethyl, acetyl, t-butyl, anisyl, benzyl, trifluoroacetyl, N-hydroxysuccinimides, t-butyloxycarbonyl, benzoyl , 4-methylbenzyl, thioanizyl, thiocresyl, benzyloxymethyl, 4-nitrophenyl, benzyloxycarbonyl, 2-nitrobenzoyl, 2-nitrophenylsulphenyl, 4-toluenesulphonyl, pentafluorophenyl, diphenylmethyl, 2-chlorobenzyloxycarbonyl, 2,4,5-trichlorophenyl, 2-bromobenzyloxycarbonyl, 9 Fluorenylmethyloxycarbonyl, tripheylmethyl, 2,2,5,7,8-pentamethylchroman-6-sulphonyl. Likewise, a derivative is to be understood as meaning the covalent or noncovalent binding of the substance to a macromolecular carrier, as well as noncovalent inclusion in suitable macromolecular cage structures. Also, couplings with other macromolecular compounds, such as polyethylene glycol, may be made. Further preferred chemical modifications are the modification of one or more of the chemical groups -COOH, -OH, = NH, -NH ₂ -SH to -COOR, -OR, -NHR, -NR 2, -NHR, -NR, -SR; in which:
R is -CH = CH-R2, -C≡C-R2, -C (R ₂ ) = CH ₂ , -C (R ₂ ) = C (R 3), -CH = NR ₂ , -C (R ₂ ) = N-R 3 , a 4-7 C-ring system with or without substitution, a 4-7 nitrogen heterocycle with or without substitution, or a C ₂ to C ₈ chain with 1 to 5 double or triple bonds with substitutions selected from R1, R2, or R3 , in which
-R 1 is H, -R, -NO _2, -CN, halide substituent, -N _3, -C1-8 alkyl, - (CH ₂₎ n CO ₂ R 2, -C2-8 alkenyl-CO ₂ R 2, -O (CH ₂ ) nCO ₂ R ₂ , -C (O) NR ₂ R 3, -P (O) (OR ₂ ) ₂ , alkyl substituted tetrazol-5-yl, - (CH ₂ ) n O (CH ₂ ) n aryl, -NR ₂ R 3, - (CH ₂₎ NOR 2, - (CH ₂₎ NSR2, -N (R2) C (O) R3, -S (O ₂₎ NR2R3, -N (R2) S (O ₂₎ R 3, - (CHR 2) nNR2R3, -C (O) R3, _(CH2) nN (R3) C (O) R3, -N (R2) CR2R3, substituted or unsubstituted _(CH2) n-cycloalkyl, substituted or unsubstituted _(CH2) n-phenyl, or cycle; where n is a number greater than 1;
-R2 is H, halide substituent, alkyl, haloalkyl, - (CH ₂₎ n-phenyl, - _(CH2) 1-3-biphenyl, - (CH ₂₎ 1-4-Ph-N (SO ₂ -C 1 -2-alkyl) _2, -CO (CHR1) n OR1, - (CHR1) n-heterocycle, - (CHR1) n-NH-CO-R1, - (CHR1) n-NH-SO ₂ R1, - ( CHR1) n-Ph-N _(SO2 -C1-2 alkyl) 2, - (CHR1) n C (O) (CHR1) -NHR1, - (CHR1) n C (S) (CHR1) -NHR1, - (CH ₂ ) nO (CH ₂ ) n CH ₃ , -CF ₃ , -C ₂ -C ₅ acyl, - (CHR 1) n OH, - (CHR 1) n CO ₂ R ₁ , - (CHR 1) nO-alkyl, - (CHR 1) nO- (CH ₂ ) nO-alkyl, - (CHR 1) n -S -alkyl, - (CHR 1) nS (O) -alkyl, - (CHR 1) nS (O ₂ ) -alkyl, - (CHR 1) nS (O ₂ ) -NHR 3 , - (CHR ₃ ) n N ₃ , - (CHR 3) n NHR 4, a C ₂ to C ₈ chain alkene chain having 1 to 5 double bonds, a C ₂ to C ₈ chain alkyne chain having 1 to 5 triple bonds, substituted or unsubstituted - (CHR3) n heterocycle, substituted or unsubstituted saturated or unsaturated - (CHR3) n cycloalkyl; where n is a number greater than 1 and R1 and R3 may be the same or different;
-R3 is H, -OH, -CN, substituted alkyl, -C ₂ -C ₈ alkenyl, substituted or unsubstituted cycloalkyl, -N (R1) R2, saturated or non-saturated C ₅ to C ₇ heterocycle, or from 4 to Heterobizyklus 7 C atoms, -NR1, -NR2, -NR1R2 consisting of a saturated or unsaturated heterocycle or a heterocycle of 4 to 7 C atoms;
-R 4 is H, - (CH ₂₎ n OH, -C (O) OR5, -C (O) SR5, - (CH ₂₎ n C (O) NR6R7, -OC (O) -O-R6, an amino acid or a peptide; where n is a number between 0 and 4;
-R5 is H,
-R6 is -C (R7) - _(CH2) nOC (O) -R 8, - (CH ₂₎ n C (R7) -OC (O) R8, - (CH ₂₎ n C (R7) -OC (O) -O-R8, or -C (R7) - _(CH2) nOC (O) -O-R8; where n is a number between 0 and 4; and
R 7 and R 8 are each H, alkyl, substituted alkyl, aryl, substituted aryl, alkenyl, substituted alkenyl, alkynyl, substituted alkynyl, heterocycle, substituted heterocycle, alkylaryl, substituted alkylaryl, cycloalkyl, substituted cycloalkyl, or CH ₂ CO ₂ alkyl, where R7 and R8 may be the same or different.

According to the invention, it is further possible to use all possible combinations of those mentioned above as belonging to i., Ii. or iii. to use said substances and / or derivatives thereof.

In another embodiment of the invention, the surfactant preparation is characterized by further comprising at least one other ingredient selected from the group consisting of builder, peroxygen compound, bleach activator, nonaqueous solvent, acid, water soluble salt, thickener, disinfecting ingredient and combinations thereof.

The addition of one or more of the further ingredient (s) proves to be advantageous, as this further improved cleaning performance and / or disinfection is achieved. Preferably, the improved cleaning performance and / or disinfection is based on a synergistic interaction of at least two ingredients. In particular, by the combination of the lipase and / or phosphonate contained therein with one of the builders described below and / or with one of the peroxygen compounds described below and / or with one of the bleach activators described below and / or with one of the nonaqueous solvents described below and / or with one of the acids described below and / or with one of the water-soluble salts described below and / or with one of the thickening agents described below and / or with one of the disinfecting ingredients described below, such a synergy can be achieved.

Builders which may be present in the surfactant preparation include, in particular, silicates, aluminum silicates (in particular zeolites), carbonates, salts of organic di- and polycarboxylic acids and mixtures of these substances.

Organic builders which may be present in the surfactant preparation are, for example, the polycarboxylic acids which can be used in the form of their sodium salts, polycarboxylic acids meaning those carboxylic acids which carry more than one acid function. These are, for example, citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids, aminocarboxylic acids, nitrilotriacetic acid (NTA), methylglycinediacetic acid (MGDA) and derivatives thereof and mixtures thereof. Preferred salts are the salts of polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, tartaric acid, sugar acids and mixtures thereof.

As builders further polymeric polycarboxylates are suitable. These are, for example, the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example, those having a molecular weight of 600 to 750,000 g / mol.

Suitable polymers are in particular polyacrylates, which preferably have a molecular weight of from 1,000 to 15,000 g / mol. Because of their superior solubility, the short-chain polyacrylates, which have molecular weights of from 1,000 to 10,000 g / mol, and particularly preferably from 1,000 to 5,000 g / mol, may again be preferred from this group.

Also suitable are copolymeric polycarboxylates, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid. To improve the water solubility, the polymers may also contain allylsulfonic acids, such as allyloxybenzenesulfonic acid and methallylsulfonic acid, as a monomer.

However, preference is given to using soluble builders, such as, for example, citric acid, or acrylic polymers having a molar mass of from 1,000 to 5,000 g / mol, preferably in the liquid surfactant preparation.

For the purposes of this document, the molecular weights stated for polymeric polycarboxylates are weight-average molecular weights M w of the particular acid form, which were determined in principle by means of gel permeation chromatography (GPC), a UV detector being used. The measurement was carried out against an external polyacrylic acid standard, which provides realistic molecular weight values due to its structural relationship with the polymers investigated. These data differ significantly from the molecular weight data, in which polystyrene sulfonic acids are used as standard. The molar masses measured against polystyrenesulfonic acids are generally significantly higher than the molecular weights specified in this document.

If desired, such organic builder substances may be present in amounts of up to 40% by weight, in particular up to 25% by weight and preferably from 1% by weight to 8% by weight. Quantities near the mentioned upper limit are preferably used in paste-like or liquid, especially hydrous, surfactant preparations.

Peroxygen compounds which are suitable for use in surfactant preparations according to the invention are, in particular, organic peracids or persalts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and inorganic salts which release hydrogen peroxide under the washing conditions, such as perborate, percarbonate, persilicate and / or persulphate Caroat belong into consideration. If a preparation contains peroxygen compounds, they are present in amounts of preferably up to 50% by weight, especially from 5% to 30% by weight. The addition of small amounts of known bleach stabilizers such as phosphonates, borates or metaborates and metasilicates and magnesium salts such as magnesium sulfate may be useful.

As bleach activators, it is possible to use compounds which, under perhydrolysis conditions, give aliphatic peroxycarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid. Suitable substances are those which carry O- and / or N-acyl groups of the stated C atom number and / or optionally substituted benzoyl groups. Preference is given to polyacylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N- Acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates, in particular n-nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy- 2,5-dihydrofuran and enol esters and also acetylated sorbitol and mannitol or their described mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfruktose, tetraacetylxylose and octaacetyllactose as well as acetylated, optionally N-alkylated glucamine and gluconolactone, and / or N- acylated lactams, for example N-benzoyl-caprolactam. The hydrophilic substituted acyl acetals and the acyl lactams are also preferably used. Combinations of conventional bleach activators can also be used. Such bleach activators can, in particular in the presence of the abovementioned hydrogen peroxide-producing bleach, in the usual amount range, preferably in amounts of from 0.5 wt .-% to 10 wt .-%, in particular 1 wt .-% to 8 wt .-%, based on However, the total surfactant preparation, be contained when using percarboxylic acid as the sole bleach, but preferably completely.

In addition to the conventional bleach activators or in their place, sulfone imines and / or bleach-enhancing transition metal salts or transition metal complexes may also be present as so-called bleach catalysts.

The surfactant preparations according to the invention are liquid and preferably contain water as the main solvent. In addition or alternatively, non-aqueous solvents may be added to the surfactant preparation. Suitable non-aqueous solvents include mono- or polyhydric alcohols, alkanolamines or glycol ethers, provided that they are miscible with water in the specified concentration range. Preferably, the solvents are selected from ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, glycerol, diglycol, propyldiglycol, butyldiglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, Propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol monomethyl ether, dipropylene glycol monoethyl ether, diisopropylene glycol monomethyl ether, di-isopropylene glycol monoethyl ether, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether, di-n-octyl ether, and the like Mixtures of these solvents. However, it is preferred that the surfactant formulation contain a polyol as a nonaqueous solvent. The polyol may in particular comprise glycerol, 1,2-propanediol, 1,3-propanediol, ethylene glycol, diethylene glycol and / or dipropylene glycol. Most preferably, the surfactant formulation contains a mixture of a polyol and a monohydric alcohol. Non-aqueous solvents may be used in the surfactant preparation in amounts of between 0.5 and 15% by weight, but preferably below 12% by weight.

To set a desired one, by mixing the rest. Components not self-resulting pH, the surfactant formulations system and environmentally acceptable acids, especially citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and / or adipic acid, but also mineral acids, especially sulfuric acid, or bases, especially ammonium - or alkali metal hydroxides. Such pH regulators are present in the surfactant preparations in amounts of preferably not more than 20% by weight, in particular from 1.2% by weight to 17% by weight.

A surfactant preparation according to the invention may further contain one or more water-soluble salts which serve, for example, for adjusting the viscosity. These may be inorganic and / or organic salts. Useful inorganic salts are preferably selected from the group consisting of colorless water-soluble halides, sulfates, sulfites, carbonates, bicarbonates, nitrates, nitrites, phosphates and / or oxides of the alkali metals, alkaline earth metals, aluminum and / or transition metals; Furthermore, ammonium salts can be used. Particularly preferred are halides and sulfates of the alkali metals; Preferably, therefore, the inorganic salt is selected from the group comprising sodium chloride, potassium chloride, sodium sulfate, potassium sulfate and mixtures thereof. Useful organic salts are, for example, colorless water-soluble alkali metal, alkaline earth metal, ammonium, aluminum and / or transition metal salts of the carboxylic acids. Preferably, the salts are selected from the group comprising formate, acetate, propionate, citrate, malate, tartrate, succinate, malonate, oxalate, lactate and mixtures thereof.

For thickening, a surfactant preparation according to the invention may contain one or more thickeners. Preferably, the thickener is selected from the group comprising xanthan, guar, carrageenan, agar-agar, gellan, pectin, locust bean gum and mixtures thereof. These compounds are effective thickeners even in the presence of inorganic salts. In a particularly preferred embodiment, the surfactant formulation contains xanthan gum as a thickener because xanthan effectively thickened even in the presence of high salt concentrations and prevents macroscopic separation of the continuous phase. In addition, the thickener stabilizes the continuous, low surfactant phase and prevents macroscopic phase separation.

Alternatively or additionally, (meth) acrylic acid (co) polymers can also be used as thickeners. be used. Suitable acrylic and methacrylic (co) polymers include, for example, the high molecular weight homopolymers of acrylic acid crosslinked with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol or propylene (INCI name according to "International Dictionary of Cosmetic Ingredients" of "The Cosmetic, Toiletry and Fragrance Association (CTFA) ": carbomer), also referred to as carboxyvinyl polymers. Such polyacrylic acids are available, among others, under the trade names Polygel ^® and Carbopol ^®. Furthermore, for example, the following acrylic acid copolymers are suitable: (i) copolymers of two or more monomers from the group of acrylic acid, methacrylic acid and their simple, preferably formed with C _1-4 alkanols, esters (INCI acrylates copolymer), for example, among the tradename Aculyn ^®, Acusol ^® or Tego ^® polymer can be obtained; (ii) crosslinked high molecular weight acrylic acid copolymers, such as those crosslinked with an allyl ether of sucrose or pentaerythritol copolymers of C _10-30 alkyl acrylates with one or more monomers selected from the group of acrylic acid, methacrylic acid and their simple, preferably C ₁₄ alkanols formed, esters (INCI acrylates / C _10-30 alkyl acrylate Crosspolymer) and which are for example available under the trade name Carbopol ^®. Other suitable polymers are (meth) acrylic acid (co) polymers of the type Sokalan ^®.

It may be preferred that the surfactant preparation according to the invention contains a (meth) acrylic acid (co) polymer in combination with a further thickener, preferably xanthan. The surfactant preparation may contain from 0.05 to 1.5% by weight and preferably from 0.1 to 1% by weight, based in each case on the total surfactant preparation, of thickeners. The amount of thickener used depends on the type of thickener and the desired degree of thickening.

In particular, ingredients which have an antimicrobial or antiviral activity, ie kill germs, are understood to be a disinfectant ingredient. The germicidal effect is dependent on the content of the disinfecting ingredient in the surfactant preparation, wherein the germicidal effect decreases with decreasing content of disinfecting ingredient or increasing dilution of the surfactant preparation.

A preferred disinfecting ingredient is ethanol or propanol. These monohydric alcohols are commonly used in disinfectants and detergents because of their solvent properties and their germicidal activity. The term "propanol" includes both the 1-propanol (n-propanol) and the 2-propanol ("isopropanol"). Ethanol and / or propanol, for example, in an amount of from 10 to 65 wt .-%, preferably 25 to 55 wt .-% in the surfactant preparation. Another preferred disinfecting ingredient is tea tree oil. These are the essential oil of the Australian Tea Tree (Melaleuca alternifolia), a native of New South Wales and Queensland evergreen shrub of the genus Myrtenheiden (Melaleuca), and other tea tree species from various genera (eg Baeckea, Kunzea and Leptospermum) in the myrtle family (Myrtaceae). The tea tree oil is made by steam distillation from the leaves and branch tips of these Trees won and is a mixture of approx. 100 substances; to. the main constituents include (+) - terpinene-4-ol, α-terpinene, terpinolene, terpineol, pinene, myrcene, phellandrene, p-cymene, limonene and 1,8-cineole. Tea tree oil is contained, for example, in an amount of 0.05 to 10% by weight, preferably 0.1 to 5.0% by weight, in the virucidal treatment solution. Another preferred disinfecting ingredient is lactic acid. The lactic acid or 2-hydroxypropionic acid is a fermentation product produced by various microorganisms. She is weakly active in antibiotics. Lactic acid is contained in the surfactant preparation, for example, in amounts of up to 10% by weight, preferably 0.2 to 5.0% by weight.

Further disinfectant ingredients are, for example, active compounds from the groups of alcohols, aldehydes, antimicrobial acids or their salts, carboxylic esters, acid amides, phenols, phenol derivatives, diphenyls, diphenylalkanes, urea derivatives, oxygen, nitrogen acetals and formals, benzamidines, isothiazoles and derivatives thereof such as isothiazolines and isothiazolinones, phthalimide derivatives, pyridine derivatives, antimicrobial surface active compounds, guanidines, antimicrobial amphoteric compounds, quinolines, 1,2-dibromo-2,4-dicyanobutane, iodo-2-propynyl-butyl-carbamate, iodine, iodophores and peroxides. Among these, preferred active ingredients are selected from the group comprising 1,3-butanediol, phenoxyethanol, 1,2-propylene glycol, glycerol, undecylenic acid, citric acid, lactic acid, benzoic acid, salicylic acid, thymol, 2-benzyl-4-chlorophenol, 2,2 '. -Methylene bis (6-bromo-4-chlorophenol), 2,4,4'-trichloro-2'-hydroxydiphenyl ether, N- (4-chlorophenyl) -N- (3,4-dichlorophenyl) -urea, N , N '- (1,10-decanediyldi-1-pyridinyl-4-ylidene) bis (1-octanamine) dihydrochloride, N, N'-bis (4-chlorophenyl) -3,12-diimino-2 , 4,11,13-tetraazatetradecandiimidamide, quaternary surface active compounds, guanidines. Preferred quaternary surface active compounds contain an ammonium, sulfonium, phosphonium, iodonium or arsonium group. Furthermore, it is also possible to use disinfecting essential oils which at the same time provide scenting of the virucidal treatment solution. However, particularly preferred active ingredients are selected from the group comprising salicylic acid, quaternary surfactants, in particular benzalkonium chloride, peroxo compounds, in particular hydrogen peroxide, alkali metal hypochlorite and mixtures thereof. Such another disinfecting ingredient is, for example, in an amount of 0.01 to 1 wt .-%, preferably 0.02 to 0.8 wt .-%, in particular 0.05 to 0.5 wt .-%, particularly preferably 0 , 1 to 0.3 wt .-%, most preferably 0.2 wt .-% in the surfactant preparation.

Liquid surfactant preparations according to the invention in the form of customary solvent-containing solutions are generally prepared by simply mixing the ingredients, which can be added in bulk or as a solution in an automatic mixer.

Surfactant preparations according to the invention may contain as enzymatic constituents exclusively a lipase as described. Alternatively, they may also contain other hydrolytic enzymes or other enzymes in a concentration useful for the effectiveness of the surfactant formulation. In a further embodiment of the invention, therefore, the surfactant preparation comprises at least one further enzyme. In principle, all the enzymes established in the prior art for this purpose can be used in this regard. Other enzymes which can be used as further enzymes are all enzymes which can display catalytic activity in a surfactant preparation according to the invention, in particular a protease, amylase, cellulase, hemicellulase, mannanase, pectinase, tannase, xylanase, xanthanase, .beta.-glucosidase, carrageenase, perhydrolase, oxidase, Oxidoreductase or another lipase, and mixtures thereof. Further enzymes are advantageously contained in the surfactant preparation in each case in a total amount of 1 × 10 ^-8 to 5 wt .-% based on active protein. More preferably, each further enzyme is in an amount of 1 × 10 ^-7 -3 wt%, from 0.00001-1 wt%, from 0.00005-0.5 wt%, from 0.0001 to 0.1 wt .-% and particularly preferably from 0.0001 to 0.05 wt .-% in inventive surfactant preparations, based on active protein. Particularly preferably, the enzymes show synergistic cleaning performance against certain stains or stains, ie the enzymes contained in the surfactant preparation support each other in their cleaning performance. Very particular preference is given to such synergism between the lipase contained and another enzyme of the surfactant preparation according to the invention, including in particular between the lipase and a protease and / or an amylase and / or a mannanase and / or a cellulase and / or a pectinase. Synergistic effects can occur not only between different enzymes, but also between one or more enzymes and other ingredients of the surfactant preparation according to the invention.

Among the proteases, those of the subtilisin type are preferable. Examples thereof are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the enzymes thermitase, proteinase K and the subtilases, but not the subtilisins in the narrower sense Proteases TW3 and TW7. Subtilisin Carlsberg in a developed form under the trade names Alcalase ^® from Novozymes A / S, Bagsvaerd, Denmark, available. The subtilisins 147 and 309 are sold under the trade names Esperase ^®, or Savinase ^® from Novozymes. From the protease from Bacillus lentus DSM 5483 derived under the name BLAP ^® protease variants derived. Other usable proteases are, for example, under the trade names Durazym ^®, relase ^®, Everlase® ^®, Nafizym ^®, Natalase ^®, Kannase® ^® and Ovozyme ^® from Novozymes, the ^® under the trade names Purafect ^®, Purafect ^® OxP, Purafect Prime, Excellase ^® and Properase.RTM ^® from Genencor, that under the trade name Protosol® ^® from Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi ^® from Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® ^® and Protease ^P® from Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan. Particular preference is also given to using the proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications WO 2008/086916 and WO 2007/131656 ,

Amylases which can be synthesized according to the invention are, for example, the α-amylases from Bacillus licheniformis, from Bacillus amyloliquefaciens or from Bacillus stearothermophilus, and in particular also their further developments improved for use in detergents or cleaners. The enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl ^® and by the company Danisco / Genencor under the name Purastar® ^® ST. Development products of this α-amylase are available from the company Novozymes under the trade names Duramyl ^® and Termamyl ^® ultra, by the company Danisco / Genencor under the name Purastar® ^® OxAm and from the company Daiwa Seiko Inc., Tokyo, Japan, as Keistase ^® available. The α-amylase from Bacillus amyloliquefaciens is marketed by the company Novozymes under the name BAN ^®, and variants derived from the α-amylase from Bacillus stearothermophilus under the names BSG ^® and Novamyl ^®, also from the company Novozymes. Furthermore, for this purpose, the α-amylase from Bacillus sp. A 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948). Likewise, fusion products of all the molecules mentioned can be used. In addition, the enhancements available under the trade names Fungamyl.RTM ^® by the company Novozymes of α-amylase from Aspergillus niger and A. oryzae, which are. Other advantageous commercial products are for example the Amylase-LT ^® and Stainzyme® ^® or ultra Stainzyme® ^® or Stainzyme® plus ^®, the latter also from the company Novozymes. Also variants of these enzymes obtainable by point mutations can be used according to the invention. Particularly preferred amylases are disclosed in International Publications WO 00/60060 . WO 03/002711 . WO 03/054177 and WO 07/079938 , whose disclosure is therefore expressly referred to, or whose disclosure in this regard is therefore expressly incorporated into the present patent application. Further, amylases which can be synthesized according to the invention are preferably .alpha.-amylases.

Examples of additional lipases or cutinases which can be synthesized according to the invention, which are contained in particular because of their triglyceride-cleaving activities, but also in order to generate in situ peracids from suitable precursors, are the lipases which are originally obtainable from, or improved, Humicola lanuginosa (Thermomyces lanuginosus), in particular those with the amino acid exchange D96L. They are sold, for example, by Novozymes under the trade names Lipolase ^®, Lipolase Ultra ^®, LipoPrime® ^®, Lipozyme® ^® and Lipex ^®. Furthermore, for example, the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens. By Genencor, for example, the lipases or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii. Other important commercial products are the originally marketed by Gist-Brocades preparations M1 Lipase ^® and Lipomax® ^® and the enzymes marketed by Meito Sangyo KK, Japan under the names Lipase MY-30 ^®, Lipase OF ^® and lipase PL ^® to mention also the product Lumafast® ^® from Genencor.

Detergents or cleaning agents according to the invention may also contain cellulases, depending on the purpose, as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously supplement each other in terms of their various performance aspects. These performance aspects include, in particular, contributions to the primary washing performance, the secondary washing performance of the composition (anti-redeposition effect or graying inhibition) and softening (fabric effect), up to the exercise of a "stone washed" effect.

According to the invention attachable cellulases (endoglucanases, EC) include, for example, fungal endoglucanase (EG) -rich cellulase preparation and developments thereof, which is offered by the company Novozymes under the trade name Celluzyme ^®. The products Endolase ^® and Carezyme ^® , also available from Novozymes, are based on the 50 kD EC, and 43 kD EG from Humicola insolens DSM 1800. Further commercial products of this company are Cellusoft® ^{®, ®} and Renozyme Cellucean ^®. Also usable are, for example cellulases, which are available from the company AB Enzymes, Finland, under the trade names Ecostone ^® and Biotouch ^®, and the at least partly based on the 20 kD EG Melanocarpus. Other cellulases from the company AB Enzymes are Econase® ^® and ECOPULP ^®. Other suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, those derived from Bacillus sp. CBS 670.93 by the company Danisco / Genencor under the trade name Puradax® ^® available. Further usable commercial products of the company Danisco / Genencor are "Genencor detergent cellulase L" and IndiAge ^® Neutra. Also variants of these enzymes obtainable by point mutations can be used according to the invention. Particularly preferred cellulases are Thielavia terrestris cellulase variants described in International Publication WO 98/12307 Cellulases from Melanocarpus, in particular Melanocarpus albomyces, disclosed in the international publication WO 97/14804 Cellulases of the EGIII type from Trichoderma reesei disclosed in the European patent application EP 1 305 432 and variations obtainable therefrom, in particular those disclosed in the European patent applications EP 1240525 and EP 1305432 , as well as cellulases, which are disclosed in international publications WO 1992006165 . WO 96/29397 and WO 02/099091 , The respective disclosure is therefore expressly referred to, or the disclosure content of which in this respect is therefore expressly included in the present patent application.

Furthermore, in particular for the removal of certain problem soiling, further enzymes can be used, which are summarized by the term hemicellulases. These include, for example, mannanases, xanthan lyases, xanthanases, pectin lyases (= pectinases), pectin esterases, pectate lyases, xyloglucanases, xylanases, pullulanases and β-glucanases. In this regard, suitable enzymes United States for example, under the name Gamanase ^® and Pektinex AR ^® from Novozymes, under the name Rohapec ^® 811 from AB Enzymes and under the name Pyrolase® ^® from Diversa Corp., San Diego, CA. , The recovered from Bacillus subtilis β-glucanase is available under the name Cereflo ^® from Novozymes. According to the invention particularly preferred hemicellulases are mannanases, which are marketed under the trade names man Away ^® by the company Novozymes or Purabrite ^® by the company Genencor.

To increase the bleaching effect, a surfactant preparation according to the invention may also contain oxidoreductases, for example oxidases, oxygenases, catalases (which react as peroxidase at low H ₂ O ₂ concentrations), peroxidases, such as halo-, chloro-, bromo-, lignin-, glucose- or manganese peroxidases, dioxygenases or laccases (phenol oxidases, polyphenol oxidases). Suitable commercial products Denilite® ^® 1 and 2 from Novozymes should be mentioned. As an example of advantageous systems for enzymatic perhydrolysis can be applied to the applications WO 98/45398 A1 . WO 2005/056782 A2 such as WO 2004/058961 A1 directed. A combined enzymatic bleaching system comprising an oxidase and a perhydrolase describes the application WO 2005/124012 , Advantageously, it is additionally preferred to add organic, particularly preferably aromatic, compounds which interact with the enzymes in order to enhance the activity of the relevant oxidoreductases (enhancers) or to ensure the flow of electrons (mediators) at greatly varying redox potentials between the oxidizing enzymes and the soils.

The enzymes to be used according to the invention may also be formulated together with accompanying substances, for example from the fermentation, or with stabilizers and incorporated in such a formulation in a surfactant preparation according to the invention.

A further subject of the invention is the use of a surfactant preparation according to the invention for the removal of stains, in particular of lipase-sensitive stains, on textiles or hard surfaces, i. H. for cleaning textiles or hard surfaces. For surfactant preparations according to the invention can be used, in particular because of the combination of phosphonate and lipase, advantageously to eliminate impurities from textiles or from hard surfaces. Embodiments of this subject invention include, for example, hand washing, manual removal of stains from textiles or hard surfaces, or use in conjunction with a machine process. All aspects, articles, and embodiments described for surfactant formulations of the invention are also applicable to this subject of the invention , Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive use. The same applies to the use of a surfactant preparation according to the invention for disinfection.

A further subject of the invention is a process for the cleaning of textiles or hard surfaces or for disinfection, wherein in at least one process step a. Inventive surfactant preparation is applied.

Another object of the invention is a process, in particular a washing, cleaning or disinfecting process, in which a wash liquor comprising a phosphonate and a lipase, which is naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus comprises , is contacted with a lipase-sensitive stain or germ on a textile or hard surface.

This includes both manual and mechanical processes, with mechanical processes being preferred on account of their more precise controllability, for example with regard to the quantities and reaction times used. Processes for cleaning textiles are generally characterized in that one or more cleaning-active substances are applied to the items to be cleaned and washed off after the action time. In particular, the cleaning product is treated with the surfactant preparation or the wash liquor formed by it, preferably for a certain minimum duration, for example 5, 10, 15, 20, 25, 30, 40, 50 or 60 minutes. The same applies to processes for cleaning all other materials than textiles, especially hard surfaces. In disinfection process, the germ to be killed is brought into contact with the surfactant preparation or the wash liquor formed by it, preferably for a certain minimum duration, for example 5, 10, 15, 20, 25, 30, 40, 50 or 60 minutes. All conceivable washing, cleaning or disinfection methods can be used in at least one of the method steps to the application of a surfactant preparation according to the invention or to the. Application of a lipase according to the invention in combination with a phosphonate are enriched and then represent embodiments of the present invention. All facts, objects and embodiments described for surfactant preparations according to the invention are also applicable to these subjects of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive method.

In a preferred embodiment, a method according to the invention is characterized in that the lipase is present in the wash liquor in a concentration of 0.0000003 to 0.0004 wt .-%, preferably from 0.0000005 to 0.0003 wt .-%, wherein the Details are based on active protein in the wash liquor. In a further preferred embodiment, a method according to the invention is characterized in that it is carried out at a temperature between 10 ° C and 80 ° C, preferably between 10 ° C and 70 ° C and more preferably between 20 ° C and 60 ° C.

Lipases provided according to the invention are advantageously usable in surfactant preparations according to the invention and processes, in particular washing, cleaning or disinfection processes. They can therefore be used advantageously to provide lipolytic activity in corresponding preparations.

A further aspect of the invention therefore provides the use of a lipase naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus, for providing a lipolytic activity in a liquid surfactant preparation further comprising a phosphonate.

Another object of the invention is the use of a lipase, which is naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus, for the removal of lipase-sensitive stains on textiles or hard surfaces or for disinfection in a wash liquor, which further comprises a phosphonate.

All facts, subjects and embodiments described for surfactant preparations and / or methods according to the invention are also applicable to the mentioned uses. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive uses.

Example:

• A: Ruß/Mineralöl auf Baumwolle: Produkt Nr. C-01 erhältlich von CFT;
• B: Ruß/Olivenöl auf Baumwolle: Produkt Nr. C-02 erhältlich von CFT;
• C: Pigment/Öl auf Baumwolle: Produkt Nr. C-09 erhältlich von CFT;
• D: Hautfett (Sebum)/Kohlenschwarz,auf Baumwolle: Produkt Nr. C-S-32 erhältlich von CFT.

Determination of the cleaning performance of a liquid surfactant preparation according to the invention For this example, standardized, dirty textiles were used, which were used by the Center For Testmaterials (CFT, Vlaardingen, Netherlands). The following stains and textiles were used:

• A: carbon black / mineral oil on cotton: Product No. C-01 available from CFT;
• B: carbon black / olive oil on cotton: Product No. C-02 available from CFT;
• C: Pigment / Oil on Cotton: Product No. C-09 available from CFT;
• D: Skin fat (sebum) / carbon black, on cotton: Product No. CS-32 available from CFT.

With this test material, various detergents were examined for their cleaning performance. For this, the batches were washed for 30 minutes at temperatures of 40 ° C. The dosage was 3.5 grams of detergent per liter of wash liquor. It was washed with city water with a water hardness of about 16 ° German hardness.

The detergent base formulation used was a phosphonate-containing liquid detergent of the following composition (all figures in percent by weight): 0.3-0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol , 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut oil. Fatty acids, 0.5% HEDP (1-hydroxyethane-1,1-diphosphonic acid), 0-0.4% PVP (polyvinylpyrrolidone), 0-0.05% optical brightener, 0-0.001% dye, balance demineralized water.

This basic detergent formulation was activity equal to 0.35 wt .-% Lipex 100L (for the different experimental series lipase preparation of the company Novozymes (batch 4 is set as a reference) with the following lipases: lipase M-AP10 ^® (Run 1), lipase LE ^® (batch 2) and Lipase ^F® (also Lipase ^JV® , batch 3), all available from Amano Pharmaceuticals.

After washing, the whiteness of the washed fabrics was measured. The measurement was carried out on a Minolta CM508d spectrometer (illuminant D65, 10 °). The device was previously calibrated with a supplied white standard. The results obtained are the difference remissions between a washing process with a detergent containing the respective lipase and a parallel control wash with a detergent without lipase.

The results are summarized in the following Table 1 and allow a direct conclusion on the contribution of each enzyme contained to the cleaning performance of the agent used. Table 1: Wash results with a liquid detergent at 40 ° C soiling Approach 1 Approach 2 Approach 3 Approach 4 A 32.6 32.2 33.3 29.7 B 32.1 31.9 32.1 27.1 C 63.2 61.9 62.1 61.2 D 31.6 31.8 32.8 30.8

It is clear that surfactant preparations according to the invention (batches 1 to 3) show very good cleaning performances, which are improved over the reference (batch 4). SEQUENCE LISTING

QUOTES INCLUDE IN THE DESCRIPTION

This list of the documents listed by the applicant has been generated automatically and is included solely for the better information of the reader. The list is not part of the German patent or utility model application. The DPMA assumes no liability for any errors or omissions.

Cited patent literature

• EP 443063 [0004]
• JP 1225490 [0004]
• WO 2008/086916 [0082]
• WO 2007/131656 [0082]
• WO 00/60060 [0083]
• WO 03/002711 [0083]
• WO 03/054177 [0083]
• WO 07/079938 [0083]
• WO 98/12307 [0086]
• WO 97/14804 [0086]
• EP 1305432 [0086, 0086]
• EP 1240525 [0086]
• WO 1992006165 [0086]
• WO 96/29397 [0086]
• WO 02/099091 [0086]
• WO 98/45398 A1 [0088]
• WO 2005/056782 A2 [0088]
• WO 2004/058961 A1 [0088]
• WO 2005/124012 [0088]

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Claims (10)

A liquid surfactant preparation comprising a phosphonate and a lipase naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus. Surfactant preparation according to Claim 1, characterized in that the phosphonate is selected from the group consisting of 1-hydroxyethane-1,1-diphosphonic acid (HEDP), aminotrimethylenephosphonic acid (ATMP), nitrilotrimethylenephosphonic acid (NTMP), diethylenetriaminepentamethylenephosphonic acid (DTPMP, DETPMP or DTPNT), ethylenediamine tetramethylenephosphonic acid (EDTMP), 2-phosphonobutane-1,2,4-tricarboxylic acid (PBS-AM) and combinations thereof. A surfactant preparation according to claim 1 or 2, characterized in that the lipase has an amino acid sequence which corresponds to that shown in SEQ ID NO. 1 amino acid sequence is at least 80% identical. A surfactant preparation according to any one of claims 1 to 3, characterized in that the phosphonate is contained in an amount of 0.01 to 4 wt .-%, and / or that the lipase in an amount of 1 × 10 ^-8 to 5 wt. -%, based on active protein. Surfactant preparation according to one of claims 1 to 4, characterized in that it is a washing, cleaning or disinfecting agent. A surfactant preparation according to any one of claims 1 to 5, characterized in that it further comprises a component selected from i. anionic and / or polyanionic substance, and / or ii. cationic and / or polycationic substance, and / or iii. Hydroxyl and / or polyhydroxyl group (s) having substance. A surfactant preparation according to any one of claims 1 to 6, characterized in that it further comprises at least one further ingredient selected from the group consisting of builder, peroxygen compound, bleach activator, nonaqueous solvent, acid, water soluble salt, thickener, disinfecting ingredient and combinations thereof, and / or that it comprises at least one further enzyme, in particular a protease, amylase, cellulase, hemicellulase, mannanase, pectinase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase, perhydrolase, oxidase, oxidoreductase or a lipase, and preferably mixtures thereof. Process for the cleaning of textiles or hard surfaces or for disinfection, characterized in that in at least one process step, a surfactant preparation according to one of claims 1 to 7 is applied. A method, in particular washing, cleaning or disinfecting method, comprising a wash liquor comprising a phosphonate and a lipase naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus, with a lipase-sensitive soiling or a germ on a textile or a hard surface is brought into contact. Use of a lipase naturally present in a microorganism, wherein the microorganism is Rhizopus oryzae or Mucor javanicus, for providing a lipolytic activity in a liquid surfactant preparation further comprising a phosphonate, or for the removal of lipase-sensitive stains on textiles or hard surfaces or for disinfection in a wash liquor, which further comprises a phosphonate.